Fluorescent castasterone reveals BRI1 signaling from the plasma membrane - PubMed (original) (raw)

doi: 10.1038/nchembio.958.

Simone Di Rubbo, Evelien Mylle, Jos Van den Begin, Joanna Schneider-Pizoń, Jaroslava Hniliková, Miroslav Šíša, Dieter Buyst, Josep Vilarrasa-Blasi, Anna-Mária Szatmári, Daniël Van Damme, Kiril Mishev, Mirela-Corina Codreanu, Ladislav Kohout, Miroslav Strnad, Ana I Caño-Delgado, Jiří Friml, Annemieke Madder, Eugenia Russinova

Affiliations

• PMID: 22561410
• DOI: 10.1038/nchembio.958

Fluorescent castasterone reveals BRI1 signaling from the plasma membrane

Niloufer G Irani et al. Nat Chem Biol. 2012.

Abstract

Receptor-mediated endocytosis is an integral part of signal transduction as it mediates signal attenuation and provides spatial and temporal dimensions to signaling events. One of the best-studied leucine-rich repeat receptor-like kinases in plants, BRASSINOSTEROID INSENSITIVE 1 (BRI1), perceives its ligand, the brassinosteroid (BR) hormone, at the cell surface and is constitutively endocytosed. However, the importance of endocytosis for BR signaling remains unclear. Here we developed a bioactive, fluorescent BR analog, Alexa Fluor 647-castasterone (AFCS), and visualized the endocytosis of BRI1-AFCS complexes in living Arabidopsis thaliana cells. Impairment of endocytosis dependent on clathrin and the guanine nucleotide exchange factor for ARF GTPases (ARF-GEF) GNOM enhanced BR signaling by retaining active BRI1-ligand complexes at the plasma membrane. Increasing the trans-Golgi network/early endosome pool of BRI1-BR complexes did not affect BR signaling. Our findings provide what is to our knowledge the first visualization of receptor-ligand complexes in plants and reveal clathrin- and ARF-GEF-dependent endocytic regulation of BR signaling from the plasma membrane.

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